ID   P2C27_ARATH             Reviewed;         380 AA.
AC   P93006;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   27-MAR-2024, entry version 148.
DE   RecName: Full=Probable protein phosphatase 2C 27 {ECO:0000303|PubMed:19021904};
DE            Short=AtPP2C27 {ECO:0000303|PubMed:19021904};
DE            EC=3.1.3.16 {ECO:0000255|PROSITE-ProRule:PRU01082};
DE   AltName: Full=Probable protein phosphatase 2C G group 1 {ECO:0000303|PubMed:22627139};
DE            Short=AtPP2CG1 {ECO:0000303|PubMed:22627139};
GN   Name=PP2C27 {ECO:0000303|PubMed:19021904};
GN   Synonyms=PP2CG1 {ECO:0000303|PubMed:22627139};
GN   OrderedLocusNames=At2g33700 {ECO:0000312|Araport:AT2G33700};
GN   ORFNames=T1B8.2 {ECO:0000312|EMBL:AAC69126.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   GENE FAMILY, AND NOMENCLATURE.
RC   STRAIN=cv. Columbia;
RX   PubMed=19021904; DOI=10.1186/1471-2164-9-550;
RA   Xue T., Wang D., Zhang S., Ehlting J., Ni F., Jacab S., Zheng C., Zhong Y.;
RT   "Genome-wide and expression analysis of protein phosphatase 2C in rice and
RT   Arabidopsis.";
RL   BMC Genomics 9:550-550(2008).
RN   [5]
RP   FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY SALT STRESS; DROUGHT AND
RP   ABSCISIC ACID, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia;
RX   PubMed=22627139; DOI=10.1016/j.bbrc.2012.05.064;
RA   Liu X., Zhu Y., Zhai H., Cai H., Ji W., Luo X., Li J., Bai X.;
RT   "AtPP2CG1, a protein phosphatase 2C, positively regulates salt tolerance of
RT   Arabidopsis in abscisic acid-dependent manner.";
RL   Biochem. Biophys. Res. Commun. 422:710-715(2012).
CC   -!- FUNCTION: Confers salt tolerance by triggering the expression of
CC       stress-responsive genes. {ECO:0000269|PubMed:22627139}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83421; EC=3.1.3.16; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU01082};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:61977; EC=3.1.3.16; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU01082};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU01082};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU01082};
CC       Note=Binds 2 magnesium or manganese ions per subunit.
CC       {ECO:0000255|PROSITE-ProRule:PRU01082};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22627139}. Cytoplasm
CC       {ECO:0000269|PubMed:22627139}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flower, and
CC       trichomes. {ECO:0000269|PubMed:22627139}.
CC   -!- INDUCTION: Induced in shoots by drought in roots by abscisic acid
CC       (ABA), and both in roots and shoot by salt stress.
CC       {ECO:0000269|PubMed:22627139}.
CC   -!- DISRUPTION PHENOTYPE: Decreased salt tolerance.
CC       {ECO:0000269|PubMed:22627139}.
CC   -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR   EMBL; U78721; AAC69126.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC08870.1; -; Genomic_DNA.
DR   EMBL; AY070460; AAL49863.1; -; mRNA.
DR   EMBL; AY091323; AAM14262.1; -; mRNA.
DR   PIR; E84748; E84748.
DR   RefSeq; NP_180926.1; NM_128928.3.
DR   AlphaFoldDB; P93006; -.
DR   SMR; P93006; -.
DR   BioGRID; 3282; 1.
DR   IntAct; P93006; 1.
DR   STRING; 3702.P93006; -.
DR   iPTMnet; P93006; -.
DR   PaxDb; 3702-AT2G33700-1; -.
DR   ProteomicsDB; 248709; -.
DR   EnsemblPlants; AT2G33700.1; AT2G33700.1; AT2G33700.
DR   GeneID; 817935; -.
DR   Gramene; AT2G33700.1; AT2G33700.1; AT2G33700.
DR   KEGG; ath:AT2G33700; -.
DR   Araport; AT2G33700; -.
DR   TAIR; AT2G33700; PP2CG1.
DR   eggNOG; KOG0698; Eukaryota.
DR   HOGENOM; CLU_013173_21_2_1; -.
DR   InParanoid; P93006; -.
DR   OMA; AQMEDEH; -.
DR   OrthoDB; 91820at2759; -.
DR   PhylomeDB; P93006; -.
DR   PRO; PR:P93006; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; P93006; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
DR   GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR   GO; GO:0009414; P:response to water deprivation; IEP:TAIR.
DR   CDD; cd00143; PP2Cc; 1.
DR   Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR   InterPro; IPR015655; PP2C.
DR   InterPro; IPR000222; PP2C_BS.
DR   InterPro; IPR036457; PPM-type-like_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR   PANTHER; PTHR13832; PROTEIN PHOSPHATASE 2C; 1.
DR   PANTHER; PTHR13832:SF673; PROTEIN PHOSPHATASE 2C 27-RELATED; 1.
DR   Pfam; PF00481; PP2C; 1.
DR   SMART; SM00331; PP2C_SIG; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; PP2C-like; 1.
DR   PROSITE; PS01032; PPM_1; 1.
DR   PROSITE; PS51746; PPM_2; 1.
DR   Genevisible; P93006; AT.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Hydrolase; Magnesium; Manganese; Metal-binding; Nucleus;
KW   Protein phosphatase; Reference proteome.
FT   CHAIN           1..380
FT                   /note="Probable protein phosphatase 2C 27"
FT                   /id="PRO_0000367956"
FT   DOMAIN          84..344
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT   BINDING         128
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         128
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         129
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         292
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         335
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   380 AA;  41757 MW;  B869BEFAE839C550 CRC64;
     MSMDFSPLLT VLEGDFNKDN TSSATEIDTL ENLDDTRQIS KGKPPRHLTS SATRLQLAAN
     ADVDVCNLVM KSLDDKSEFL PVYRSGSCAE QGAKQFMEDE HICIDDLVNH LGAAIQCSSL
     GAFYGVFDGH GGTDAAHFVR KNILRFIVED SSFPLCVKKA IKSAFLKADY EFADDSSLDI
     SSGTTALTAF IFGRRLIIAN AGDCRAVLGR RGRAIELSKD HKPNCTAEKV RIEKLGGVVY
     DGYLNGQLSV ARAIGDWHMK GPKGSACPLS PEPELQETDL SEDDEFLIMG CDGLWDVMSS
     QCAVTIARKE LMIHNDPERC SRELVREALK RNTCDNLTVI VVCFSPDPPQ RIEIRMQSRV
     RRSISAEGLN LLKGVLDGYP
//